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MGC > Protien Molecules > Flashcards

Protien Molecules Flashcards

1
Q

What bonds are amino acids linked by

A

Covalent bonds in linear chain

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2
Q

Primary structure of proteins

A

Linear amino acid sequence

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3
Q

Secondary structure of proteins

A

Polypeptide folding into regular shapes (forms domains)

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4
Q

Tertiary protein structure

A

Arrangement of one or more domains (3D structure)

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5
Q

Quaternary protein structure

A

Arrangement of multiple polypeptide chains in one protein - forms protein complex with subunits

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6
Q

What are domains

A

How elements of secondary structure are packed together

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7
Q

What is the alpha carbon in an amino acid

A

Linked to amino group (-NH2), a carboxyl group (-COOH), a alpha hydrogen atom and an R group (chiral carbon)

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8
Q

What form do amino acids exist in neutral pH

A

Zwitterion form at neutral pH

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9
Q

What does the formation of a dipeptide from two amino acids results in

A

Loss of water - condensation reaction

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10
Q

What is a residue

A

Each amino acid unit of polypeptide chain called a residue

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11
Q

What structure do peptide bonds adopt

A

Rigid planar structure

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12
Q

How are disulphide bonds formed

A

Between side chains of two cysteine residues under oxidising conditions

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13
Q

How can disulphide bonds be cleaved

A

By reducing agents such as B (beta) - mercaptoe thanol

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14
Q

What are histones composed of

A

DNA packaging - many Arg, Lys => very basic proteins

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15
Q

What are membrane proteins composed of

A

Many Leu, Val and ile = > hydrophobic proteins

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16
Q

What amino acids compose extracellular proteins

A

Many Cys to form disulphide bond, stable protein

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17
Q

What is a result of cis configuration of side chains

A

Neighbouring amino acids can result in steric hinderance

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18
Q

Types of non covalent bonds

A

Hydrogen bonds
Salt bridges (electrostatic interaction)
Vẫn đẻr waals interaction

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19
Q

What are Hydrogen bonds essential for

A

Crucial for protein folding and formation of secondary structure

20
Q

Formation of salt bridges and their importance

A

-Formed by attractive forces between oppositely charged atoms
- important in quaternary structure formation

21
Q

Where do Hydrogen bonds form on secondary structure of protein

A

Between -Nh and -CO groups on different but adjacent strands

22
Q

What are the two main secondary structures of a protein

A

Alpha helixes (a-helices)
Beta sheet (B-sheet)

23
Q

What are tertiary structures composed of

A

‘Bundles’ (aka domains) of secondary structures

24
Q

Characteristics of a domain

A

-hydrophilic side chains exposed
-hydrophobic side chains buried in hydrophobic core

25
Q

What is a domain

A

Region of polypeptide chain that folds independently and self stabilising

26
Q

How do polypeptide chains fold

A

Fold spontaneously in aqueous environment

27
Q

What does the hydrophobic effect drive

A

Drives formation of hydrophobic core proteins and promotes tertiary structure formation

28
Q

What are the 3 classes of domain structures

A

-alpha helical domains
-beta sheet domains
-alpha/beta domains

29
Q

Characteristics of alpha helical domains

A

packed together in bundles or ‘coiled -coil’

30
Q

What do common domains consist of

A

-pair of helices
-connected by short loop
-packed in anti parallel arrangement

31
Q

What is a beta sandwich and it’s characteristics

A

-two beta sheets packed together
-stabilised by ‘fillings’ - hydrophobic side chains

32
Q

What is the B - barrel and its characteristics

A

-eight b -strands may form closed ‘barrel’ structure (Chinese finger trap looking like)
Hydrophobic residues orientated towards centre of barrel

33
Q

What is the Ross man fold

A

Beta strand and alpha helical repeats

34
Q

In clonal selection what happens to activated B cells

A

B cell clone will proliferate and differentiate into antibody secreting cells

35
Q

What is innate immunity

A

Rapid but non-specific

36
Q

What is adaptive immunity

A

Based on lymphocyte with antigen receptors - immunological memory

37
Q

What is the epitope

A

The antigenic determinant and site where antibody binds to on the antigen

38
Q

What is neutralisation in immunity

A

Binding of antibodies to epitope on surface of pathogens prevents entry to host cells

39
Q

What is opsonisation in immunity

A

The coating of a pathogen with molecules like antibodies and increases efficiency of phagocytosis

40
Q

What agglutination in immunity

A

The process of the clumping of pathogens driven by interaction of antibody with antigens and prevents spread of pathogens through the system

41
Q

What is the complement cascade in immunity

A

Antibody-antigen complex stimulates binding of Cl => activation of protease that triggers chains of amplification cascade

42
Q

What is antibody dependant cellular cytotoxicity in immunology

A

Mechanism where large pathogens are killed by secretion of cytotoxic

43
Q

What is the stimulation of cytokine release in immunology

A

IgE antibodies bind to receptors on mast cells and basophils => antigen binding to IgE on these cells stridulate the secretion of cytokines and histamine

44
Q

What does histamine do

A

Causes vasodilation and leafiness in blood vessels - its release causes allergic reactions

45
Q

What are IgE antibodies produced in response to

A

Response to parasites and environmental allergens e.g pollen, food and drugs

46
Q

What is the structure of immunoglobulin (Ig)/antibody)

A

-4 polypeptide chains - two heavy (H) chains
- two light (L) chains
-linked by disulphide bonds

MGC (7 decks)

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